ID   F0NQR5_SULIH            Unreviewed;       236 AA.
AC   F0NQR5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000256|ARBA:ARBA00011890};
DE            EC=2.1.1.77 {ECO:0000256|ARBA:ARBA00011890};
GN   OrderedLocusNames=SiH_2670 {ECO:0000313|EMBL:ADX84007.1};
OS   Sulfolobus islandicus (strain HVE10/4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX84007.1, ECO:0000313|Proteomes:UP000006395};
RN   [1] {ECO:0000313|EMBL:ADX84007.1, ECO:0000313|Proteomes:UP000006395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX84007.1,
RC   ECO:0000313|Proteomes:UP000006395};
RX   PubMed=21278296; DOI=10.1128/JB.01487-10;
RA   Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA   Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA   Huang L., Garrett R.A.;
RT   "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT   organisms for genetic and virus-host interaction studies.";
RL   J. Bacteriol. 193:1672-1680(2011).
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC       in peptides and proteins that result from spontaneous decomposition of
CC       normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC       repair and/or degradation of damaged proteins.
CC       {ECO:0000256|ARBA:ARBA00025330}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC         [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC         COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC         ChEBI:CHEBI:90598; EC=2.1.1.77;
CC         Evidence={ECO:0000256|ARBA:ARBA00029295};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005369}.
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DR   EMBL; CP002426; ADX84007.1; -; Genomic_DNA.
DR   RefSeq; WP_014513340.1; NC_017275.1.
DR   AlphaFoldDB; F0NQR5; -.
DR   GeneID; 78427641; -.
DR   KEGG; sih:SiH_2670; -.
DR   HOGENOM; CLU_055432_2_0_2; -.
DR   Proteomes; UP000006395; Chromosome.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:ADX84007.1};
KW   Transferase {ECO:0000313|EMBL:ADX84007.1}.
SQ   SEQUENCE   236 AA;  27122 MW;  88225E83F6E926B0 CRC64;
     MSAKEDLLRS IKNSKLANAF IKVNREDFLP QLLKKYAYDP NYIDKPFYVT PNITTTALSL
     GIYILDILNL EENQKVLEIG TGIGYYTALI AEVVGENNVV SIEIDDTMFE YAKNVLLIRY
     PLIKLIKMDG SLGYEREAPY DRIVIWAAAP TIPCKLYEQL KENGIMVAPI GSEKAQGLYR
     ITRIGYEPKI ERIGDVIFMK MRGLFGFYED DDPNERRIKK IEEKVNRLLS KFMNQS
//